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Protein

Glutathione S-transferase

Gene

gst

Organism
Ochrobactrum anthropi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Kineticsi

  1. KM=0.132 mM for glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glutathione1 Publication
    Binding sitei35 – 351Glutathione1 Publication
    Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei105 – 1051Glutathione1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase (EC:2.5.1.18)
    Gene namesi
    Name:gst
    OrganismiOchrobactrum anthropi
    Taxonomic identifieri529 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. 1 Publication
    Mutagenesisi11 – 111S → A: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Glutathione S-transferasePRO_0000185973Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi439375.Oant_1298.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54Combined sources
    Helixi12 – 2110Combined sources
    Beta strandi26 – 294Combined sources
    Turni32 – 354Combined sources
    Helixi43 – 453Combined sources
    Beta strandi54 – 585Combined sources
    Beta strandi61 – 655Combined sources
    Helixi66 – 7510Combined sources
    Helixi80 – 823Combined sources
    Helixi89 – 10921Combined sources
    Helixi110 – 1123Combined sources
    Helixi118 – 13821Combined sources
    Beta strandi148 – 1503Combined sources
    Helixi153 – 16715Combined sources
    Helixi176 – 18611Combined sources
    Helixi189 – 1979Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NTOX-ray2.10A1-201[»]
    2PVQX-ray1.80A1-201[»]
    ProteinModelPortaliP81065.
    SMRiP81065. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81065.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8181GST N-terminalAdd
    BLAST
    Domaini87 – 201115GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 662Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Beta family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13409. GST_N_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81065-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG
    60 70 80 90 100
    AVPALEVKPG TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF
    110 120 130 140 150
    CSDLHAAFSG LFAPNLSEEA RAGVIANINR RLGQLEAMLS DKNAYWLGDD
    160 170 180 190 200
    FTQPDAYASV IIGWGVGQKL DLSAYPKALK LRERVLARPN VQKAFKEEGL

    N
    Length:201
    Mass (Da):21,739
    Last modified:May 30, 2000 - v2
    Checksum:i763B2D3DECA21F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1.
    RefSeqiWP_010659377.1. NZ_KK073936.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1.
    RefSeqiWP_010659377.1. NZ_KK073936.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NTOX-ray2.10A1-201[»]
    2PVQX-ray1.80A1-201[»]
    ProteinModelPortaliP81065.
    SMRiP81065. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi439375.Oant_1298.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4382.

    Miscellaneous databases

    EvolutionaryTraceiP81065.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13409. GST_N_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi."
      Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.
      Biochem. J. 335:573-579(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, MUTAGENESIS.
    2. "Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi."
      Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.
      FEMS Microbiol. Lett. 160:81-86(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25.
    3. "Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site."
      Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.
      Proteins 71:16-23(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGST_OCHAN
    AccessioniPrimary (citable) accession number: P81065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: June 24, 2015
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.